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First published online 9 June 2009
doi: 10.1242/jcs.042747

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Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for targeting of the TuRC to the centrosome

¹ The MOE Key Laboratory of Cell Proliferation and Differentiation and the State Key Laboratory of Bio-membrane and Membrane Bio-engineering, College of Life Sciences, Peking University, Beijing 100871, China
² Proteomics Platform, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100871, China
³ Department of Biological Sciences, California State Polytechnic University, Pomona, CA 91768, USA

^* Author for correspondence (e-mail: zhangcm{at}pku.edu.cn)

Accepted 1 April 2009

Nedd1 is a new member of the -tubulin ring complex (TuRC) and targets the TuRC to the centrosomes for microtubule nucleation and spindle assembly in mitosis. Although its role is known, its functional regulation mechanism remains unclear. Here we report that the function of Nedd1 is regulated by Cdk1 and Plk1. During mitosis, Nedd1 is firstly phosphorylated at T550 by Cdk1, which creates a binding site for the polo-box domain of Plk1. Then, Nedd1 is further phosphorylated by Plk1 at four sites: T382, S397, S637 and S426. The sequential phosphorylation of Nedd1 by Cdk1 and Plk1 promotes its interaction with -tubulin for targeting the TuRC to the centrosome and is important for spindle formation. Knockdown of Plk1 by RNAi decreases Nedd1 phosphorylation and attenuates Nedd1 accumulation at the spindle pole and subsequent -tubulin recruitment at the spindle pole for microtubule nucleation. Taken together, we propose that the sequential phosphorylation of Nedd1 by Cdk1 and Plk1 plays a pivotal role in targeting TuRC to the centrosome by promoting the interaction of Nedd1 with the TuRC component -tubulin, during mitosis.

Key words: Cdk1, Nedd1, Plk1, Centrosome, Phosphorylation, TuRC

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